Histone-H4 (acLys5) antibody

Antigen: Histone-H4

Binding Site: acLys5

Clonality: Monoclonal

Host: Rabbit

Reactivity: Human, Rat (Rattus)

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunoprecipitation (IP)

Certificates: ISO 9001:2008

Catalog no.: ABIN649866

Additional Information

Gene ID: 8363, 8362, 8359, 8365, 8360, 121504, 8361, 8366,

UniProt: P62805

Characteristics: Rabbit Monoclonal Antibody

Specificity: A synthetic peptide corresponding to residues near the N-terminus of human Histone H4 was used as an immunogen.

Molecular Weight: 11 kDA

Comments:

Background: Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Acetylation of histone H4 thus appears to play a primary role in the structural changes that mediate enhanced binding of transcription factors to their recognition sites within nucleosomes (3). Histone H4 can be reversibly acetylated at lysine residues 5, 8, 12 and 16. It has been shown that, in H4 from human cells, the four lysine residues are acetylated in a preferred, but not exclusive order, namely lysine 16, followed by 12 and 8, followed by 5 (4).

Application Details

Application Notes: The suggested dilution is: WB: ~~ 1:10000~50000 IP: ~~ 1:50 ICC: ~~ 1:250~500 IHC: ~~ 1:250~500

Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Storage: Histone-H4 Antibody Acetyl (K5) can be stored at -20°C for up to 12 months from time of receipt.

Research Area: Ubiquitin-related antibodies, Signaling, Phospho-specific antibodies, Protein Modifications, Transcription Factors, Chromatin, Cell Structure

Restrictions: For Research Use only

Publications

Product: Vettese-Dadey, Grant, Hebbes et al.: "Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro." in: The EMBO journal, Vol. 15, Issue 10, pp. 2508-18, 1996 (PubMed).

Braunstein, Sobel, Allis et al.: "Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern." in: Molecular and cellular biology, Vol. 16, Issue 8, pp. 4349-56, 1996 (PubMed).

Workman, Kingston: "Alteration of nucleosome structure as a mechanism of transcriptional regulation." in: Annual review of biochemistry, Vol. 67, pp. 545-79, 1998 (PubMed).